메뉴 건너뛰기




Volumn 41, Issue 6-7, 2007, Pages 835-841

Purification and characterization of a novel protease-resistant α-galactosidase from Rhizopus sp. F78 ACCC 30795

Author keywords

Alpha galactosidase; Characterization; Protease resistant; Rhizopus sp.

Indexed keywords

GALACTOSIDASES; GUAR GUM; PROTEASE RESISTANT; STACHYOSE;

EID: 34548456824     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2007.07.005     Document Type: Article
Times cited : (35)

References (39)
  • 1
    • 0015269593 scopus 로고
    • Biochemistry of α-galactosidase
    • Dey P.M., and Pridham J.B. Biochemistry of α-galactosidase. Adv Enzynol 36 (1972) 91-130
    • (1972) Adv Enzynol , vol.36 , pp. 91-130
    • Dey, P.M.1    Pridham, J.B.2
  • 2
    • 0035807420 scopus 로고    scopus 로고
    • Multiple α-galactosidases from Aspergillus niger: purification, characterization and substrate specificities
    • Ademark P., Larsson M., Tjerneld F., and Stalbrand H. Multiple α-galactosidases from Aspergillus niger: purification, characterization and substrate specificities. Enzyme Microb Technol 29 (2001) 441-448
    • (2001) Enzyme Microb Technol , vol.29 , pp. 441-448
    • Ademark, P.1    Larsson, M.2    Tjerneld, F.3    Stalbrand, H.4
  • 3
    • 0000920026 scopus 로고
    • Production of fungal α-galactosidase and its application to hydrolysis of galactooligosaccharides in soybean milk
    • Cruz R., and Park Y.K. Production of fungal α-galactosidase and its application to hydrolysis of galactooligosaccharides in soybean milk. J Food Sci 47 (1982) 1973-1975
    • (1982) J Food Sci , vol.47 , pp. 1973-1975
    • Cruz, R.1    Park, Y.K.2
  • 4
    • 0029553390 scopus 로고
    • Ramalingam. Enzymic hydrolysis of raffinose and stachyose in soymilk by alpha-galactosidase from Gibberella fujikuroi
    • Mulimani V.H. Ramalingam. Enzymic hydrolysis of raffinose and stachyose in soymilk by alpha-galactosidase from Gibberella fujikuroi. Biochem Mol Biol Int 36 (1995) 897-905
    • (1995) Biochem Mol Biol Int , vol.36 , pp. 897-905
    • Mulimani, V.H.1
  • 5
    • 0000045271 scopus 로고
    • Effect of soaking, cooking and crude α-galactosidase treatment on the oligosaccharide content of cowpea flours
    • Somiari R.I., and Balogh E. Effect of soaking, cooking and crude α-galactosidase treatment on the oligosaccharide content of cowpea flours. Sci Food Agric 61 (1993) 339-343
    • (1993) Sci Food Agric , vol.61 , pp. 339-343
    • Somiari, R.I.1    Balogh, E.2
  • 6
    • 0033949347 scopus 로고    scopus 로고
    • A comparison of enzyme-aided bleaching of softwood paper pulp using combinations of xylanase, mannanase and α-galactosidase
    • Clarke J.H., Davidson K., Rixon J.E., Halstead J.R., Fransen M.P., Gilbert H.J., et al. A comparison of enzyme-aided bleaching of softwood paper pulp using combinations of xylanase, mannanase and α-galactosidase. Appl Microbiol Biotechnol 53 (2000) 661-667
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 661-667
    • Clarke, J.H.1    Davidson, K.2    Rixon, J.E.3    Halstead, J.R.4    Fransen, M.P.5    Gilbert, H.J.6
  • 7
    • 0027138967 scopus 로고
    • Enzymatic hydrolysis of isolated and fibre-bound galactoglucomannans from pine-wood and pine kraft pulp
    • Rättö M., Siika-aho M., Buchert J., Valkeajävi A., and Viikari L. Enzymatic hydrolysis of isolated and fibre-bound galactoglucomannans from pine-wood and pine kraft pulp. Appl Microbiol Biotechnol 40 (1993) 449-454
    • (1993) Appl Microbiol Biotechnol , vol.40 , pp. 449-454
    • Rättö, M.1    Siika-aho, M.2    Buchert, J.3    Valkeajävi, A.4    Viikari, L.5
  • 8
    • 0020126902 scopus 로고
    • Immobilized α-d-galactosidase in the sugar beet industry
    • Linden J.C. Immobilized α-d-galactosidase in the sugar beet industry. Enzyme Microb Technol 4 (1982) 130-136
    • (1982) Enzyme Microb Technol , vol.4 , pp. 130-136
    • Linden, J.C.1
  • 9
    • 0028213906 scopus 로고
    • Transfusions to group O subjects of 2 units of red cells enzymatically converted from group B to group O
    • Lenny L.L., Hurst R., Goldstein J., and Galbraith R.A. Transfusions to group O subjects of 2 units of red cells enzymatically converted from group B to group O. Transfusion 34 (1994) 209-214
    • (1994) Transfusion , vol.34 , pp. 209-214
    • Lenny, L.L.1    Hurst, R.2    Goldstein, J.3    Galbraith, R.A.4
  • 10
    • 0033673087 scopus 로고    scopus 로고
    • Expression and characterization of glycosylated and catalytically active recombinant human α-galactosidase a produced in Pichia pastoris
    • Chen Y., Jin M., Egborge T., Coppola G., Andre J., and Calhoun D.H. Expression and characterization of glycosylated and catalytically active recombinant human α-galactosidase a produced in Pichia pastoris. Protein Exp Purif 20 (2000) 472-484
    • (2000) Protein Exp Purif , vol.20 , pp. 472-484
    • Chen, Y.1    Jin, M.2    Egborge, T.3    Coppola, G.4    Andre, J.5    Calhoun, D.H.6
  • 11
    • 12944265457 scopus 로고    scopus 로고
    • Infusion of α-galactosidase A reduces tissue globotriaosylceramide storage in patients with Fabry disease
    • Schiffmann R., Murray G.J., Treco D.P., Daniel M., Sellos-Moura M., Myers M.J., et al. Infusion of α-galactosidase A reduces tissue globotriaosylceramide storage in patients with Fabry disease. Proc Natl Acad Sci USA 97 (2000) 365-370
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 365-370
    • Schiffmann, R.1    Murray, G.J.2    Treco, D.P.3    Daniel, M.4    Sellos-Moura, M.5    Myers, M.J.6
  • 12
  • 13
    • 20944441182 scopus 로고    scopus 로고
    • Cloning and expression of the gene encoding Streptomyces coelicolor A3(2) alpha-galactosidase belonging to family 36
    • Kondoh K., Morisaki K., Kim W., Park G., Kaneko S., and Kobayashi H. Cloning and expression of the gene encoding Streptomyces coelicolor A3(2) alpha-galactosidase belonging to family 36. Biotechnol Lett 27 (2005) 641-647
    • (2005) Biotechnol Lett , vol.27 , pp. 641-647
    • Kondoh, K.1    Morisaki, K.2    Kim, W.3    Park, G.4    Kaneko, S.5    Kobayashi, H.6
  • 14
    • 0032520207 scopus 로고    scopus 로고
    • Substrate specificities of Penicillium simplicissimum α-galactosidases
    • Luonteri E., Tenkanen M., and Viikari L. Substrate specificities of Penicillium simplicissimum α-galactosidases. Enzyme Microb Technol 22 (1998) 192-198
    • (1998) Enzyme Microb Technol , vol.22 , pp. 192-198
    • Luonteri, E.1    Tenkanen, M.2    Viikari, L.3
  • 15
    • 33847675844 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel α-galactosidase gene from Penicillium sp. F63 CGMCC 1669 and expression in Pichia pastoris
    • Mi S., Meng K., Wang Y., Bai Y., Yuan T., Luo H., et al. Molecular cloning and characterization of a novel α-galactosidase gene from Penicillium sp. F63 CGMCC 1669 and expression in Pichia pastoris. Enzyme Microb Technol 40 (2007) 1373-1380
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1373-1380
    • Mi, S.1    Meng, K.2    Wang, Y.3    Bai, Y.4    Yuan, T.5    Luo, H.6
  • 16
    • 0034681556 scopus 로고    scopus 로고
    • Purification of α-galactosidase from Aspergillus niger for application in the synthesis of complex oligosaccharides
    • Scigelova M., and Crout D.H.G. Purification of α-galactosidase from Aspergillus niger for application in the synthesis of complex oligosaccharides. J Mol Catal B Enzym 8 (2000) 175-181
    • (2000) J Mol Catal B Enzym , vol.8 , pp. 175-181
    • Scigelova, M.1    Crout, D.H.G.2
  • 18
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: an integrated database approach
    • Gilbert H.J., Davies G., Henrissat B., and Svensson B. (Eds), The Royal Society of Chemistry, London
    • Coutinho P.M., and Henrissat B. Carbohydrate-active enzymes: an integrated database approach. In: Gilbert H.J., Davies G., Henrissat B., and Svensson B. (Eds). Recent advances in carbohydrate bioengineering (1999), The Royal Society of Chemistry, London 3-12
    • (1999) Recent advances in carbohydrate bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 20
    • 0019503418 scopus 로고
    • Induction, isolation, and characterization of Aspergillus niger mutant strains producing elevated levels of α-galactosidase
    • Nevalainen K.M.H. Induction, isolation, and characterization of Aspergillus niger mutant strains producing elevated levels of α-galactosidase. Appl Environ Microbiol 41 (1981) 593-596
    • (1981) Appl Environ Microbiol , vol.41 , pp. 593-596
    • Nevalainen, K.M.H.1
  • 21
    • 0032055401 scopus 로고    scopus 로고
    • Characterization of galactosidases from Aspergillus niger: purification of a novel-galactosidase activity
    • Manzanares P., de Graaff L.H., and Visser J. Characterization of galactosidases from Aspergillus niger: purification of a novel-galactosidase activity. Enzyme Microb Technol 22 (1998) 383-390
    • (1998) Enzyme Microb Technol , vol.22 , pp. 383-390
    • Manzanares, P.1    de Graaff, L.H.2    Visser, J.3
  • 22
    • 0027287853 scopus 로고
    • Conditions of formation, purification, and characterization of α-galactosidase of Trichoderma reesei RUT C-30
    • Zeilinger S., Kristufek D., Arisan-Atac I., Hodits R., and Kubicek C.P. Conditions of formation, purification, and characterization of α-galactosidase of Trichoderma reesei RUT C-30. Appl Environ Microbiol 59 (1993) 1347-1353
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1347-1353
    • Zeilinger, S.1    Kristufek, D.2    Arisan-Atac, I.3    Hodits, R.4    Kubicek, C.P.5
  • 23
  • 24
    • 0037373344 scopus 로고    scopus 로고
    • Molecular cloning of endo-d-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae
    • Moriya T., Murashima K., Nakane A., Yanai K., Sumida N., Koga J., et al. Molecular cloning of endo-d-1,4-glucanase genes, rce1, rce2, and rce3, from Rhizopus oryzae. J Bacteriol 185 (2003) 1749-1756
    • (2003) J Bacteriol , vol.185 , pp. 1749-1756
    • Moriya, T.1    Murashima, K.2    Nakane, A.3    Yanai, K.4    Sumida, N.5    Koga, J.6
  • 25
    • 0026539865 scopus 로고
    • Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes
    • Yanai K., Takaya N.N., Kojima Horiuchi H., Ohta A., and Takagi M. Purification of two chitinases from Rhizopus oligosporus and isolation and sequencing of the encoding genes. J Bacteriol 174 (1992) 7398-7406
    • (1992) J Bacteriol , vol.174 , pp. 7398-7406
    • Yanai, K.1    Takaya, N.N.2    Kojima Horiuchi, H.3    Ohta, A.4    Takagi, M.5
  • 26
    • 23744488193 scopus 로고    scopus 로고
    • Enhanced reactivity of Rhizopus oryzae lipase displayed on yeast cell surface in organic solvents: Potential as a whole cell biocatalyst in organic solvents
    • Shiraga S., Kawakami M., Ishiguro M., and Ueda M. Enhanced reactivity of Rhizopus oryzae lipase displayed on yeast cell surface in organic solvents: Potential as a whole cell biocatalyst in organic solvents. Appl Environ Microbiol 71 (2005) 4335-4338
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4335-4338
    • Shiraga, S.1    Kawakami, M.2    Ishiguro, M.3    Ueda, M.4
  • 27
    • 0034090166 scopus 로고    scopus 로고
    • Isolation and expression of lactate dehydrogenase genes from Rhizopus oryzae
    • Skory C.D. Isolation and expression of lactate dehydrogenase genes from Rhizopus oryzae. Appl Environ Microbiol 66 (2000) 2343-2348
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2343-2348
    • Skory, C.D.1
  • 28
    • 84982024062 scopus 로고
    • Induction of alpha-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum
    • Dey P.M., Patel S., and Brownleader M.D. Induction of alpha-galactosidase in Penicillium ochrochloron by guar (Cyamopsis tetragonobola) gum. Biotechnol Appl Biochem 17 (1993) 361-371
    • (1993) Biotechnol Appl Biochem , vol.17 , pp. 361-371
    • Dey, P.M.1    Patel, S.2    Brownleader, M.D.3
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 34548428507 scopus 로고
    • A native PAGE staining method for α-galactosidase
    • Wu S., and Su T.Z. A native PAGE staining method for α-galactosidase. Chin J Microbiol 22 (1995) 253-254
    • (1995) Chin J Microbiol , vol.22 , pp. 253-254
    • Wu, S.1    Su, T.Z.2
  • 32
    • 33845545784 scopus 로고
    • A novel thermostable α-galactosidase from the thermophilic fungus Thermomyces lanuginosus CBS 395.62/b: purification and characterization
    • Rezessy-Szabo J.M., Nguyen Q.D., Hoschke A., Braet C., Hajos G., and Claeyssens M. A novel thermostable α-galactosidase from the thermophilic fungus Thermomyces lanuginosus CBS 395.62/b: purification and characterization. Biochim Biophys Acta 2007 (1770) 55-62
    • (1770) Biochim Biophys Acta , vol.2007 , pp. 55-62
    • Rezessy-Szabo, J.M.1    Nguyen, Q.D.2    Hoschke, A.3    Braet, C.4    Hajos, G.5    Claeyssens, M.6
  • 34
    • 0041077684 scopus 로고    scopus 로고
    • Purification and characterization of α-d-galactosidase from Bifidobacterium breve
    • Xiao M., Liu S.F., Zhu C.R., and Qia X.M. Purification and characterization of α-d-galactosidase from Bifidobacterium breve. Chin J Microbiol Immunol 21 (2001) 307-311
    • (2001) Chin J Microbiol Immunol , vol.21 , pp. 307-311
    • Xiao, M.1    Liu, S.F.2    Zhu, C.R.3    Qia, X.M.4
  • 35
    • 0014478342 scopus 로고
    • Determination of blood glucose using an oxidase peroxidase system with a non-carcinogenic chromogen
    • Tinder P. Determination of blood glucose using an oxidase peroxidase system with a non-carcinogenic chromogen. J Clin Pathol 22 (1969) 158-161
    • (1969) J Clin Pathol , vol.22 , pp. 158-161
    • Tinder, P.1
  • 36
    • 0023005968 scopus 로고
    • Production, purification, and characterization of α-galactosidase from Monascus pilosus
    • Wong H.C., Hu C.A., Yen H.L., Su W.C., Lu H.C., and Lin C.F. Production, purification, and characterization of α-galactosidase from Monascus pilosus. Appl Environ Microbiol 52 (1986) 1147-1152
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1147-1152
    • Wong, H.C.1    Hu, C.A.2    Yen, H.L.3    Su, W.C.4    Lu, H.C.5    Lin, C.F.6
  • 37
    • 0033118394 scopus 로고    scopus 로고
    • Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase
    • Brumer H., Sims P.F.G., and Sinnott M.L. Lignocellulose degradation by Phanerochaete chrysosporium: purification and characterization of the main α-galactosidase. J Biochem 339 (1999) 43-53
    • (1999) J Biochem , vol.339 , pp. 43-53
    • Brumer, H.1    Sims, P.F.G.2    Sinnott, M.L.3
  • 38
    • 0035318077 scopus 로고    scopus 로고
    • Purification and characterization of the recombinant Thermus sp. strain T2 α-galactosidase expressed in Escherichia coli
    • Ishiguro M., Kaneko K., Kuno A., Koyama Y., Yoshida S., Park G.G., et al. Purification and characterization of the recombinant Thermus sp. strain T2 α-galactosidase expressed in Escherichia coli. Appl Environ Microbiol 67 (2001) 1601-1606
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1601-1606
    • Ishiguro, M.1    Kaneko, K.2    Kuno, A.3    Koyama, Y.4    Yoshida, S.5    Park, G.G.6
  • 39
    • 0037827688 scopus 로고    scopus 로고
    • Crystal structure of rice α-galactosidase complexed with d-galactose
    • Fujimoto Z., Kaneko S., Momma M., Kobayashi H., and Mizuno H. Crystal structure of rice α-galactosidase complexed with d-galactose. J Biol Chem 278 (2003) 20313-20318
    • (2003) J Biol Chem , vol.278 , pp. 20313-20318
    • Fujimoto, Z.1    Kaneko, S.2    Momma, M.3    Kobayashi, H.4    Mizuno, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.